Glycation—a sweet tempter for neuronal death

Kikuchi, S

doi:10.1016/s0165-0173(02)00273-4

Cited by 169Advanced Glycation End Products researchGlycosylation and Glycoproteins ResearchPotato Plant Research

Glycation—a sweet tempter for neuronal death

Kikuchi, S·2003·Brain Research Reviews

DOI 10.1016/s0165-0173(02)00273-4

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Abstract

Glycation, one of the post-translational modifications of proteins, is a nonenzymatic reaction initiated by the primary addition of a sugar aldehyde or ketone to the amino groups of proteins. In the early stage of glycation, the synthesis of intermediates leading to the formation of Amadori compounds occurs. In the late stage, advanced glycation end products (AGE) are irreversibly formed after a complex cascade of reactions. Several AGEs have been characterized chemically, while other new compounds remain to be identified. To date, studies of the contribution of glycation to diseases have been primarily focused on its relationship to diabetes and diabetes-related complications. However, glucose-induced damage is not limited to diabetic patients. Although it does not cause rapid or remarkable cell damage, glycation advances slowly and accompanies every fundamental process of cellular metabolism. It has recently become clear that glycation also affects physiological aging and neurodegenerative diseases such as Alzheimer's disease and amyotrophic lateral sclerosis. Glycation alters the biological activity of proteins and their degradation processes. Protein cross-linking by AGE results in the formation of detergent-insoluble and protease-resistant aggregates. Such aggregates may interfere with both axonal transport and intracellular protein traffic in neurons. In addition, glycation reactions lead to the production of reactive oxygen species. Conversely, glycation is promoted by oxidative stress. We speculate on the presence of synergism between glycation and oxidative stress. In this review, we provide an outline of glycation and propose some possible mechanisms of its cytotoxicity and defense systems against it.

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AGEs can be formed through the polyol pathway and lipid peroxidation in the presence and absence of hyperglycemia.
“In addition to nonenzymatic glycation, AGEs can be formed through the polyol pathway and lipid peroxidation in the presence and absence of hyperglycemia, depending on the substrate type, reactant concentration, exposure time, and host cellular context14–17.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [15]

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Advanced Glycation End Products and Diabetic Complications
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Authors: Kikuchi, S.
Affiliations: Hokkaido University (JP)
Corresponding author: Kikuchi, S
Venue: Brain Research Reviews
Publisher: Elsevier BV
Published: 2003-03
Volume: 41
Issue: 2-3
Pages: 306-323
ISSN: 0165-0173 (ISSN-L)
DOI: 10.1016/s0165-0173(02)00273-4
OpenAlex: W1997719996
Cited by: 169
References: 117
Citations by year: 2026: 4 · 2025: 3 · 2024: 1 · 2023: 9 · 2022: 4 · 2021: 6 · 2020: 6 · 2019: 5 · 2018: 4 · 2017: 4 · 2016: 8 · 2015: 3 · 2014: 14 · 2013: 10 · 2012: 8
FWCI: 6.25
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Brain Research Reviews (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
Keywords: glycation, advanced glycation end products, Amadori compounds, neuronal cell death, neurodegenerative diseases, Alzheimer's disease, amyotrophic lateral sclerosis, protein cross-linking, protein aggregates, axonal transport, oxidative stress, reactive oxygen species, aging, diabetes complications, post-translational modification, cytotoxicity
MeSH terms: Animals, Glucose, Humans, Nerve Tissue Proteins, Nervous System, Neurons, Cell Death, Glycation End Products, Advanced, Reactive Oxygen Species, Oxidative Stress, Neurodegenerative Diseases

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Glycation—a sweet tempter for neuronal death

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